9KM0
Cryo-EM structure of a tri-heme cytochrome-associated RC-LH1 complex from a marine photoheterotrophic bacterium, purified with EDTA-2Na-containing solutions
This is a non-PDB format compatible entry.
Summary for 9KM0
| Entry DOI | 10.2210/pdb9km0/pdb |
| EMDB information | 62419 |
| Descriptor | Antenna pigment protein alpha chain, (21R,24R,27S)-24,27,28-trihydroxy-18,24-dioxo-19,23,25-trioxa-24lambda~5~-phosphaoctacosan-21-yl (9Z)-octadec-9-enoate, DODECYL-BETA-D-MALTOSIDE, ... (16 entities in total) |
| Functional Keywords | photosynthesis, reaction center, energy transfer |
| Biological source | Dinoroseobacter shibae DFL 12 = DSM 16493 More |
| Total number of polymer chains | 39 |
| Total formula weight | 436564.75 |
| Authors | |
| Primary citation | Wang, W.,Liu, Y.,Gu, J.,An, S.,Ma, C.,Gao, H.,Jiao, N.,Shen, J.R.,Beatty, J.T.,Koblizek, M.,Zhang, X.,Zheng, Q.,Chen, J.H. Cryo-EM Analysis of a Tri-Heme Cytochrome-Associated RC-LH1 Complex from the Marine Photoheterotrophic Bacterium Dinoroseobacter Shibae. Adv Sci, :e2413456-e2413456, 2025 Cited by PubMed Abstract: The reaction center-light harvesting 1 (RC-LH1) complex converts solar energy into electrical energy, driving the initiation of photosynthesis. The authors present a cryo-electron microscopy structure of the RC-LH1 isolated from a marine photoheterotrophic bacterium Dinoroseobacter shibae. The RC comprises four subunits, including a three-heme cytochrome (Cyt) c protein, and is surrounded by a closed LH ring composed of 17 pairs of antenna subunits. Notably, a novel subunit with an N-terminal "helix-turn-helix" motif embedded in the gap between the RC and the LH ring is identified. The purified RC-LH1 complex exhibits high stability in solutions containing Mg or Ca. The periplasmic Cyt c is predicted to bind at the junction between the Cyt subunit and the membrane plane, enabling electron transfer from Cyt c to the proximal heme of the tri-heme Cyt, and subsequently to the special pair of bacteriochlorophylls. These findings provide structural insights into the efficient energy and electron transfer processes within a distinct type of RC-LH1, and shed light on evolutionary adaptations of photosynthesis. PubMed: 40112203DOI: 10.1002/advs.202413456 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.78 Å) |
Structure validation
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